1nha

Solution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF

Method: SOLUTION NMR Dmax: 42.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Transcription initiation factor IIF, alpha subunit

Homo sapiens

UniProt P35269

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 436–517 Fragment:C-Terminal Domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;300 K;Ionic strength (raw mmCIF value) 20mM sodium phosphate buffer;Pressure ambient NMR sample composition:1mM cterRAP74 unlabeled, 20mM sodium phosphate, and 1mM EDTA | 100% D2O NMR sample composition:1mM cterRAP74 U-15N, 20mM sodium phosphate, and 1mM EDTA | 90% H2O/10% D2O NMR sample composition:1mM cterRAP74 U-15N and U-13C, 20mM sodium phosphate, and 1mM EDTA | 90% H2O/10% D2O NMR sample composition:1mM cterRAP74 U-15N and U-13C, 20mM sodium phosphate, and 1mM EDTA | 100% D2O Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

60 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T2FA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–82; UniProt 436–517

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1nha

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nha
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nha
Deposition date deposition_date2002-12-19
Structure title titleSolution Structure of the Carboxyl-Terminal Domain of RAP74 and NMR Characterization of the FCP-Binding Sites of RAP74 and CTD of RAP74, the subunit of Human TFIIF
Keywords keywordsTRANSCRIPTION FACTOR, HUMAN GENERAL TRANSCRIPTION FACTOR TFIIF, RAP74, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.76
Radius of gyration Rg (electron density) rg_electron12.22
Forward intensity I(0) i0339171000.00
Molecular weight molecular_weight157950.0 kDa
Excluded volume excluded_volume199810 ų
Envelope volume envelope_volume20177 ų
Hydration-shell volume shell_volume12331 ų
Envelope diameter envelope_diameter47.3
Shell Rg shell_rg19.61
Envelope Rg envelope_rg14.19
Shape Rg shape_rg12.17
Total Rg total_rg12.58
Total atoms total_atoms22880
Residues n_residues1340
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax42.7
Rg (real space) rg_real12.71
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real3.3920e+08
I(0) uncertainty (real space) i0_real_error3.3590e+06
Rg (reciprocal space) rg_reciprocal12.71
I(0) (reciprocal space) i0_reciprocal339200000.0000
Solution quality estimate total_estimate0.8631
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.1
Skewness Skewness skewness0.139
Kurtosis Kurtosis kurtosis-0.288
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha77080.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1nhaa_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.30 — C-terminal domain of the rap74 subunit of TFIIF

CATH v4.4 (1 domains)

Domain ID domain_id1nhaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)